Evidence map›Paper›PMID 42782431›Full record

ArticleApplied biochemistry and biotechnology2026

A Novel GH26 β-Mannanase from Bacillus subtilis HM7 Producing Manno-Oligosaccharides with Strain-Specific Prebiotic Activity.

Kornwarin Chumnankul, Nichada Apaphant, Nattanicha Tribamrung, Thanapon Charoenwongpaiboon, Karan Wangpaiboon, Weerapong Woraprayote, Wonnop Visessanguan, Rath Pichyangkura

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Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

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8 authors.

Kornwarin ChumnankulDepartment of Biochemistry, Faculty of Science, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand.
Nichada ApaphantSchool of Integrated Science, Faculty of Science, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand.
Nattanicha TribamrungDepartment of Biochemistry, Siriraj Metabolomics and Phenomics Center (SiMPC), Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, Thailand.
Thanapon CharoenwongpaiboonDepartment of Chemistry, Faculty of Science, Silpakorn University, Nakhon Pathom, 73000, Thailand.
Karan WangpaiboonCenter of Excellence in Structural and Computational Biology, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
Weerapong WoraprayoteDepartment of Biochemistry, Siriraj Metabolomics and Phenomics Center (SiMPC), Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, Thailand.
Wonnop VisessanguanDepartment of Biochemistry, Siriraj Metabolomics and Phenomics Center (SiMPC), Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, Thailand.
Rath PichyangkuraDepartment of Biochemistry, Faculty of Science, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Rath.p@chula.ac.th.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mannan-oligosaccharide (MOS) produced from the hydrolysis of mannan by β-mannanase, demonstrate several beneficial properties, such as prebiotic and modulation of tight junction activity. In this study, two novel GH26 β-mannanases, MAN26HM7/A and MAN26HM7/B, from Bacillus subtilis HM7 were cloned and expressed in Escherichia coli BL21 (DE3). The optimal pH and temperature of MAN26HM7/A and MAN26HM7/B were pH 5.0 and 40 °C, and pH 6.0 and 60 °C, respectively. The β-mannanases from Bacillus subtilis HM7 exhibited different MOS product patterns from DP2-DP6 oligo-mannose. MAN26HM7/A and MAN26HM7/B preferentially hydrolyzed substrates with more than five mannose residues. The amino acid residues, A146, F65, and H331 surrounding the active sites of MAN26HM7/A and MAN26HM7/B were compared with those of other β-mannanases from Bacillus species. These amino acid differences may be responsible for altered substrate binding, substrate specificity, and hydrolytic product pattern of MAN26HM7/A and MAN26HM7/B. MOS produced from konjac, copra meal and green coffee bean by MAN26HM7, MAN26HM7/A, and MAN26HM7/B were tested for prebiotic activity. MOS produced from coffee bean hydrolyzed by MAN26HM7/B exhibited the highest prebiotic activity score on Lacticaseibacillus rhamnosus GG (ATCC 53103). This study provides an understanding of the characteristics, hydrolysis pattern of the novel GH26 β-mannanases, and the application of these novel GH26 β-mannanase for prebiotic production from agricultural products.

Indexed as

Bacillus subtilisbeta-MannosidaseMannansOligosaccharidesPrebioticsHydrogen-Ion ConcentrationHydrolysisSubstrate SpecificityTemperaturebeta-MannosidaseMannansOligosaccharidesPrebioticsBioactiveCarbohydrate enzymeFunctional oligosaccharidesMannanMannan-degrading enzymePrebiotic

Identifiers

PMID42782431

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